1gv8: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1gv8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GV8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1gv8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GV8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aov|1aov]], [[1dot|1dot]], [[1ovb|1ovb]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gv8 OCA], [https://pdbe.org/1gv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gv8 RCSB], [https://www.ebi.ac.uk/pdbsum/1gv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gv8 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gv8 OCA], [https://pdbe.org/1gv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gv8 RCSB], [https://www.ebi.ac.uk/pdbsum/1gv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gv8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TRFE_ANAPL TRFE_ANAPL]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.  Ovotransferrin has a bacteriostatic function. Its concentration in avian egg is the highest concentration of any transferrin in vivo (By similarity).  
[https://www.uniprot.org/uniprot/TRFE_ANAPL TRFE_ANAPL] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.  Ovotransferrin has a bacteriostatic function. Its concentration in avian egg is the highest concentration of any transferrin in vivo (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gv8 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gv8 ConSurf].
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== Publication Abstract from PubMed ==
In a previous paper [Lindley et al. (1993), Acta Cryst. D49, 292-304], the X-ray structure analysis of the 18 kDa fragment of duck ovotransferrin, corresponding to the NII domain of the intact protein, was reported at a resolution of 2.3 A. In this structure, the Fe(III) cation binds to two tyrosine residues and the synergistic carbonate anion in an identical manner to that found in the intact protein. However, the aspartate and histidine residues, normally involved in iron binding in transferrins, are absent in the fragment and it was not possible to unequivocally define what had replaced them. The electron density was tentatively assigned to be a mixture of peptides, presumably resulting from the proteolytic preparation of the fragment, binding to the iron through their amino and carboxylate termini. A more recent X-ray analysis of the fragment, from a different preparation, has resulted in a structure at 1.95 A, in which glycine appears to be the predominant residue bound to the cation. In an alternative attempt to clarify the binding of iron to the 18 kDa fragment, the metal was removed by dialysis and replaced in the form of ferric nitrilotriacetate. Crystallization of this complex has resulted in an X-ray structure at 1.90 A in which the Fe(III) is bound to the synergistic carbonate anion and only one tyrosine residue in a manner almost identical to the intact protein. The carboxylate groups and the tertiary amino group of the nitrilotriacetate occupy the remaining coordination sites. The second tyrosine residue, Tyr95, is not bound directly to the iron. The implication of these structures with respect to the mechanism of iron binding by the transferrins is addressed.
The mechanism of iron uptake by transferrins: the X-ray structures of the 18 kDa NII domain fragment of duck ovotransferrin and its nitrilotriacetate complex.,Kuser P, Hall DR, Haw ML, Neu M, Evans RW, Lindley PF Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):777-83. Epub 2002, Apr 26. PMID:11976488<ref>PMID:11976488</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1gv8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transferrin 3D structures|Transferrin 3D structures]]
*[[Transferrin 3D structures|Transferrin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anas platyrhynchos]]
[[Category: Anas platyrhynchos]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hall, D R]]
[[Category: Hall DR]]
[[Category: Haw, M L]]
[[Category: Haw ML]]
[[Category: Kuser, P]]
[[Category: Kuser P]]
[[Category: Lindley, P F]]
[[Category: Lindley PF]]
[[Category: Neu, M]]
[[Category: Neu M]]
[[Category: Glycoprotein]]
[[Category: Iron transport]]
[[Category: Metal-binding]]
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